Results 211 to 220 of about 62,836 (259)
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Trends in Microbiology, 1998
Catabolite repression is a central multigene regulatory network that enables bacteria to select and utilize the optimal carbon and energy sources available in a given environment. Cyclic AMP and catabolite gene activator protein (CAP) play central roles in mediating catabolite repression in enteric bacteria but are absent from Gram-positive bacteria ...
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Catabolite repression is a central multigene regulatory network that enables bacteria to select and utilize the optimal carbon and energy sources available in a given environment. Cyclic AMP and catabolite gene activator protein (CAP) play central roles in mediating catabolite repression in enteric bacteria but are absent from Gram-positive bacteria ...
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Archives of Biochemistry and Biophysics, 1979
Abstract The plastidic ferredoxin-NADP + reductase from the xanthophycean alga Bumilleriopsis forms a stoichiometric 1:1 complex with ferredoxin and NADP + which is demonstrated by difference spectra of both complexes. Butanedione modification of the flavoprotein results in loss of its enzymatic activities (transhydrogenase and diaphorase ...
G, Bookjans, P, Böger
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Abstract The plastidic ferredoxin-NADP + reductase from the xanthophycean alga Bumilleriopsis forms a stoichiometric 1:1 complex with ferredoxin and NADP + which is demonstrated by difference spectra of both complexes. Butanedione modification of the flavoprotein results in loss of its enzymatic activities (transhydrogenase and diaphorase ...
G, Bookjans, P, Böger
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Analogues of NADP+ as inhibitors and coenzymes for NADP+ malic enzyme from maize leaves
Photosynthesis Research, 1991Structural analogues of the NADP(+) were studied as potential coenzymes and inhibitors for NADP(+) dependent malic enzyme from Zea mays L. leaves. Results showed that 1, N(6)-etheno-nicotinamide adenine dinucleotide phosphate (∈ NADP(+)), 3-acetylpyridine-adenine dinucleotide phosphate (APADP(+)), nicotinamide-hypoxanthine dinucleotide phosphate (NHDP(+
C P, Spampinato +3 more
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Archives of Biochemistry and Biophysics, 2003
The apparent equilibrium constant of the biochemical reaction, 2-propanol+NADP(ox) = acetone+NADP(red), was determined at I = 0.25 M over a wide range of pH (5.63 to 8.02) and temperature (5 to 40 degrees C). The reaction was catalyzed by an NADP-dependent alcohol dehydrogenase.
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The apparent equilibrium constant of the biochemical reaction, 2-propanol+NADP(ox) = acetone+NADP(red), was determined at I = 0.25 M over a wide range of pH (5.63 to 8.02) and temperature (5 to 40 degrees C). The reaction was catalyzed by an NADP-dependent alcohol dehydrogenase.
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Crystal Structures of a Ferredoxin: NADP+ Reductase and of a Complex with NADP+
Biochemical Society Transactions, 1996L, Serre +5 more
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Complex formation of ferredoxin-NADP reductase with ferredoxin and with NADP
Biochemical and Biophysical Research Communications, 1968M, Shin, A S, Pietro
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Journal of Biological Inorganic Chemistry, 1999
Marta Martínez-Júlvez +2 more
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Marta Martínez-Júlvez +2 more
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Structure of ferredoxin-NADP+ oxidoreductase and the location of the NADP binding site
Journal of Molecular Biology, 1981Steven Sheriff, Jon R. Herriott
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Comparison of Thio-NADP⊕and Seleno-NADP⊕in NADP⊕-Dependent Oxidoreductases
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1970WOLFRAM CHRIST +2 more
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